Τίτλος:
Osirisynes G-I, New Long-Chain Highly Oxygenated Polyacetylenes from the Mayotte Marine Sponge Haliclona sp.
Γλώσσες Τεκμηρίου:
Αγγλικά
Περίληψη:
Chemical study of the CH2Cl2ôMeOH (1:1) extract from the sponge Haliclona sp. collected in Mayotte highlighted three new long-chain highly oxygenated polyacetylenes, osirisynes G-I (1-3) together with the known osirisynes A (4), B (5), and E (6). Their structures were elucidated by 1D and 2D NMR spectra and HRESIMS and MS/MS data. All compounds were evaluated on catalase and sirtuin 1 activation and on CDK7, proteasome, Fyn kinase, tyrosinase, and elastase inhibition. Five compounds (1; 3-6) inhibited proteasome kinase and two compounds (5-6) inhibited CDK7 and Fyn kinase. Osirisyne B (5) was the most active compound with IC50 on FYNB kinase, CDK7 kinase, and proteasome inhibition of 18.44M, 9.13M, and 0.26M, respectively. © 2020 MDPI AG. All rights reserved.
Συγγραφείς:
Campos, P.-E.
Herbette, G.
Chendo, C.
Clerc, P.
Tintillier, F.
Voogd, N.J.D.
Papanagnou, E.-D.
Trougakos, I.P.
Jerabek, M.
Bignon, J.
Go, G.L.
Ouazzani, J.
Gauvin-Bialecki, A.
Λέξεις-κλειδιά:
catalase; cyclin dependent kinase 7; elastase; monophenol monooxygenase; osirisyne A; osirisyne B; osirisyne E; osirisyne G; osirisyne H; osirisyne I; polyacetylene derivative; proteasome; protein kinase Fyn; sirtuin 1; staurosporine; unclassified drug; proteasome; proteasome inhibitor, Article; biological activity; carbon nuclear magnetic resonance; controlled study; drug isolation; drug structure; enzyme activation; enzyme inhibition; Haliclona; IC50; liquid chromatography-mass spectrometry; marine invertebrate; Mayotte; nonhuman; nuclear magnetic resonance spectroscopy; proton nuclear magnetic resonance; animal; chemistry; drug effect; electrospray mass spectrometry; pharmacology; structure activity relation, Animals; Haliclona; Inhibitory Concentration 50; Magnetic Resonance Spectroscopy; Polyacetylene Polymer; Proteasome Endopeptidase Complex; Proteasome Inhibitors; Spectrometry, Mass, Electrospray Ionization; Structure-Activity Relationship
